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Literature summary for 2.4.1.19 extracted from

  • Li, Z.; Huang, M.; Gu, Z.; Holler, T.; Cheng, L.; Hong, Y.; Li, C.
    Asp577 mutations enhance the catalytic efficiency of cyclodextrin glycosyltransferase from Bacillus circulans (2016), Int. J. Biol. Macromol., 83, 111-116 .
    View publication on PubMed
Search for more literature for 2.4.1.19

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli JM109 cells Niallia circulans

Protein Variants

Protein Variants Comment Organism
D577A the mutation increases the beta-cyclization activity of the enzyme (23% higher catalytic efficiency compared to the wild type) Niallia circulans
D577G the mutation increases the beta-cyclization activity of the enzyme (43.9% higher catalytic efficiency compared to the wild type) Niallia circulans
D577I the mutation decreases the beta-cyclization activity of the enzyme (14.5% lower catalytic efficiency compared to the wild type) Niallia circulans
D577L the mutation decreases the beta-cyclization activity of the enzyme (8.8% lower catalytic efficiency compared to the wild type) Niallia circulans
D577V the mutation decreases the beta-cyclization activity of the enzyme (18.8% lower catalytic efficiency compared to the wild type) Niallia circulans

Organism

Organism UniProt Comment Textmining
Niallia circulans P43379
-
-
Niallia circulans STB01 P43379
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
maltodextrin + glycosyl acceptor
-
 Niallia circulans beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
 ?
maltodextrin + glycosyl acceptor
-
 Niallia circulans STB01 beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
 ?
soluble starch + glycosyl acceptor
-
 Niallia circulans beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
 ?
soluble starch + glycosyl acceptor
-
 Niallia circulans STB01 beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin
-
 ?

Synonyms

Synonyms Comment Organism
CGTase
-
 Niallia circulans
cyclodextrin glycosyltransferase
-
 Niallia circulans

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
371
-
 maltodextrin mutant enzyme D577G, at pH 6.5 and 50°C Niallia circulans
403
-
 maltodextrin wild type enzyme, at pH 6.5 and 50°C Niallia circulans
406
-
 maltodextrin mutant enzyme D577A, at pH 6.5 and 50°C Niallia circulans
467
-
 maltodextrin mutant enzyme D577V, at pH 6.5 and 50°C Niallia circulans
513
-
 maltodextrin mutant enzyme D577I, at pH 6.5 and 50°C Niallia circulans
583
-
 maltodextrin mutant enzyme D577L, at pH 6.5 and 50°C Niallia circulans